Evidence map›Paper›PMID 19783858›Full record

ArticleThe Journal of biological chemistry2009

Lipase maturation factor LMF1, membrane topology and interaction with lipase proteins in the endoplasmic reticulum.

Mark H Doolittle, Saskia B Neher, Osnat Ben-Zeev, Jo Ling-Liao, Ciara M Gallagher, Maryam Hosseini, Fen Yin, Howard Wong, Peter Walter, Miklós Péterfy

RetractedOpen access · hybridAbstract readRetracted Publication
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.2field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Purification, cellular levels, and functional domains of lipase maturation factor 1.Biochemical and biophysical research communications · 2014
    Article
  8. Article
  9. Article
  10. Article
  11. Genetic determinants of plasma triglycerides.Journal of lipid research · 2011
    Review
  12. Review
  13. Review
  14. Mechanisms of lipase maturation.Clinical lipidology · 2010
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 1 country.

Mark H DoolittleDepartment of Medicine, David Geffen School of Medicine, University of California, Los Angeles, California 90095, USA. markdool@ucla.edu
Saskia B Neher
Osnat Ben-Zeev
Jo Ling-Liao
Ciara M Gallagher
Maryam Hosseini
Fen Yin
Howard Wong
Peter Walter
Miklós Péterfy
Cedars-Sinai Medical Center · USUniversity of California, Los Angeles · USUniversity of California, San Francisco · USHoward Hughes Medical Institute · US

Funding

Systems genomics of metabolic syndrome traitsP01HL028481 · NHLBI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REUE, KAREN · 1985 to 2019
$50.2M
NHLBI NIH HHS HL24841NHLBI NIH HHS P01 HL028481
6 · The paper itself

Abstract

Lipase maturation factor 1 (LMF1) is predicted to be a polytopic protein localized to the endoplasmic reticulum (ER) membrane. It functions in the post-translational attainment of enzyme activity for both lipoprotein lipase and hepatic lipase. By using transmembrane prediction methods in mouse and human orthologs, models of LMF1 topology were constructed and tested experimentally. Employing a tagging strategy that used insertion of ectopic glycan attachment sites and terminal fusions of green fluorescent protein, we established a five-transmembrane model, thus dividing LMF1 into six domains. Three domains were found to face the cytoplasm (the amino-terminal domain and loops B and D), and the other half was oriented to the ER lumen (loops A and C and the carboxyl-terminal domain). This representative model shows the arrangement of an evolutionarily conserved domain within LMF1 (DUF1222) that is essential to lipase maturation. DUF1222 comprises four of the six domains, with the two largest ones facing the ER lumen. We showed for the first time, using several naturally occurring variants featuring DUF1222 truncations, that Lmf1 interacts physically with lipoprotein lipase and hepatic lipase and localizes the lipase interaction site to loop C within DUF1222. We discuss the implication of our results with regard to lipase maturation and DUF1222 domain structure.

Indexed as

Amino Acid SequenceAnimalsBinding SitesBlotting, WesternCell LineEndoplasmic ReticulumGreen Fluorescent ProteinsHeLa CellsHumansLipaseLipoprotein LipaseMembrane ProteinsMiceMicroscopy, ConfocalModels, BiologicalMutationGreen Fluorescent ProteinsLipaseLIPC protein, humanLipc protein, mouseLipoprotein LipaseLMF1 protein, humanLMF1 protein, mouseMembrane ProteinsRecombinant Fusion Proteins

Identifiers

PMID19783858
PMCPMC2785204
OpenAlexW1993263858

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.